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IGDC3_MOUSE
ID   IGDC3_MOUSE             Reviewed;         813 AA.
AC   Q8BQC3; O70246; Q792T2; Q9Z2S6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Immunoglobulin superfamily DCC subclass member 3;
DE   AltName: Full=Putative neuronal cell adhesion molecule;
DE   Flags: Precursor;
GN   Name=Igdcc3; Synonyms=Punc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 599-735 (ISOFORM 2), DEVELOPMENTAL STAGE, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster;
RX   PubMed=9507132; DOI=10.1016/s0925-4773(98)00005-7;
RA   Salbaum J.M.;
RT   "Punc, a novel mouse gene of the immunoglobulin superfamily, is expressed
RT   predominantly in the developing nervous system.";
RL   Mech. Dev. 71:201-204(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 599-735 (ISOFORMS 1 AND 2), AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=FVB/NJ;
RX   PubMed=9922388; DOI=10.1007/s003359900953;
RA   Salbaum J.M.;
RT   "Genomic structure and chromosomal localization of the mouse gene Punc.";
RL   Mamm. Genome 10:107-111(1999).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BQC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BQC3-2; Sequence=VSP_012321;
CC   -!- TISSUE SPECIFICITY: Detected in cerebellum, kidney, heart, lung,
CC       skeletal muscle and spleen. {ECO:0000269|PubMed:9507132,
CC       ECO:0000269|PubMed:9922388}.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed in embryos from 9.5 dpc to 10.5
CC       dpc. Expression is much lower at 11.5 dpc and virtually extinct at 15.5
CC       dpc. Detected in neural tube and lateral mesoderm at 9.5 dpc. At 10.5
CC       dpc detected in fore and hind limb buds and lateral plate mesoderm,
CC       throughout the neural tube, in mesencephalon and dorsal diencephalon.
CC       {ECO:0000269|PubMed:9507132}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC       {ECO:0000305}.
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DR   EMBL; AK051027; BAC34502.1; -; mRNA.
DR   EMBL; BC053057; AAH53057.1; -; mRNA.
DR   EMBL; AF026465; AAD12133.1; -; mRNA.
DR   EMBL; AF026466; AAD12123.1; -; Genomic_DNA.
DR   EMBL; AF026466; AAD12124.1; -; Genomic_DNA.
DR   CCDS; CCDS52835.1; -. [Q8BQC3-2]
DR   CCDS; CCDS90599.1; -. [Q8BQC3-1]
DR   RefSeq; NP_033014.1; NM_008988.2. [Q8BQC3-2]
DR   RefSeq; XP_006510936.1; XM_006510873.2.
DR   AlphaFoldDB; Q8BQC3; -.
DR   SMR; Q8BQC3; -.
DR   IntAct; Q8BQC3; 1.
DR   MINT; Q8BQC3; -.
DR   STRING; 10090.ENSMUSP00000034961; -.
DR   GlyGen; Q8BQC3; 7 sites.
DR   iPTMnet; Q8BQC3; -.
DR   PhosphoSitePlus; Q8BQC3; -.
DR   PaxDb; Q8BQC3; -.
DR   PRIDE; Q8BQC3; -.
DR   ProteomicsDB; 267217; -. [Q8BQC3-1]
DR   ProteomicsDB; 267218; -. [Q8BQC3-2]
DR   Antibodypedia; 2652; 43 antibodies from 12 providers.
DR   DNASU; 19289; -.
DR   Ensembl; ENSMUST00000034961; ENSMUSP00000034961; ENSMUSG00000032394. [Q8BQC3-2]
DR   Ensembl; ENSMUST00000217371; ENSMUSP00000149084; ENSMUSG00000032394. [Q8BQC3-1]
DR   GeneID; 19289; -.
DR   KEGG; mmu:19289; -.
DR   UCSC; uc009qcv.1; mouse. [Q8BQC3-2]
DR   UCSC; uc009qcw.1; mouse. [Q8BQC3-1]
DR   CTD; 9543; -.
DR   MGI; MGI:1202390; Igdcc3.
DR   VEuPathDB; HostDB:ENSMUSG00000032394; -.
DR   eggNOG; KOG4221; Eukaryota.
DR   eggNOG; KOG4222; Eukaryota.
DR   GeneTree; ENSGT00940000156969; -.
DR   HOGENOM; CLU_018612_2_0_1; -.
DR   InParanoid; Q8BQC3; -.
DR   OMA; CGLMEGK; -.
DR   OrthoDB; 1010015at2759; -.
DR   PhylomeDB; Q8BQC3; -.
DR   TreeFam; TF321506; -.
DR   BioGRID-ORCS; 19289; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Igdcc3; mouse.
DR   PRO; PR:Q8BQC3; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BQC3; protein.
DR   Bgee; ENSMUSG00000032394; Expressed in embryonic post-anal tail and 96 other tissues.
DR   Genevisible; Q8BQC3; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 6.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..813
FT                   /note="Immunoglobulin superfamily DCC subclass member 3"
FT                   /id="PRO_0000014921"
FT   TRANSMEM        653..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          49..151
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          151..232
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          250..333
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          341..428
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          438..532
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          535..630
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        172..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        271..319
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        363..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         631..650
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9507132,
FT                   ECO:0000303|PubMed:9922388"
FT                   /id="VSP_012321"
SQ   SEQUENCE   813 AA;  86460 MW;  C707194FF617A916 CRC64;
     MAEPRTASPR RLPALRRPGF LPPLLPPPPP PLLLLLLLLP LPAPSLGLGH SAELAFSVEP
     NDDIANPGQP IVLGCKVEGT PPVQVSWRKN GAELPEGTHT TLLANGSLLI HHFRLEQGGS
     PSDEGDYECV AQNRFGLLVS RKARLQAATM SDFHVHPQAV TGEEGGVARF QCQIHGLPKP
     LITWEKNRVP IDTDDERYTL LPKGVLQITG LRAEDSGIFH CVASNIASVR VSHGARLTVS
     GSGSGTYKEP TILVGPENLT LTVHQTAVLE CVATGNPRPI VSWSRLDGRP IGVEGIQVLG
     TGNLIISDVT VQHSGVYVCA ANRPGTRVRR TAQGRLVVQA PAEFVQHPQS ISRPAGTTAM
     FTCQAQGEPP PHVTWLKNGQ VLGAGGHVRL KNNNSTLSIS GVGPEDEAIY QCVAENIAGS
     SQASARLTVL WAEGLPGPPR NVRAVSVSST EVRVSWSEPL AHTKEIIGYV LHIRKAADSP
     KLEYQEAVSK STFQHLVRDL EPSTAYSFYI KAYTPRGASL ASVPTLASTL GEAPVPPPLS
     VRLLGSSSLQ LLWKPWPRLA QHNGGFKLFY RPVSATSFTG PILLPGTVSS YNLSQLDPST
     VYEVKLLAYN QHGDGNATVR FVSLKGASER TALTPPCDCR KEDVTNHTST TGIVIGIHIG
     VTCIIFCVLF LLFGQRGRVL LCKDVENQLS PPQGPRSQRD PGILALNGLS RGEGGQLSRD
     EKPVDAKELE QLFPTAGSAA QPGSTPTDPA APAPCEETQL SMVQLQGFNL VAGRTTEATS
     PCAGPGPVPA PQDIGPVPLS EGQTQPPAVA APQ
 
 
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